Instrumentation is requested to establish a facility for molecular graphics display within the Department of Chemistry. The major user group consists of six faculty members. Each investigator is currently involved in projects that require the visualization of complex molecular structures with the aid of computer graphics equipment. Four of the contributors are interested in the enzymatic and physical properties of wild type and mutant proteins, whereas two are focusing on smaller organic molecules. Investigation of the factors underlying catalysis and substrate binding of several classes of enzymes: DNA polymerase I, DNA gyrase, T4 polymerase complex, dihydrofolate reductase and trifunctional enzymes in the de novo pathway for purine biosynthesis. Template directed organic synthesis, focusing on the design of rigid template molecules to facilitate reactions of organic substrates. New strategies for the rational synthesis of polycarbocyclic ring systems. Application of this methodology in the synthesis of bioactive natural products and analogs. Stability and folding pattern of apo b type hemeproteins and selected mutants, determination of structural features of proteins in solution using high-resolution nuclear magnetic resonance stectroscopy. Mechanism by which the primary structure of a protein directs the rapid and efficient folding to the native conformation. Site-directed mutagenesis is used to target individual amino acids in the alpha subunit of tryptophan synthase and dihydrofolate reductase. Understanding catalysis and regulation of several enzymes that are focal points in biosynthetic pathways. The factors that couple catalysis and changes in protein structure due to regulation by protein modification are being investigated by site-directed mutagenesis of the catalytic and regulatory sites.